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Protein

Methyl-CpG-binding domain protein 2

Gene

MBD2

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds CpG islands in promoters where the DNA is methylated at position 5 of cytosine within CpG dinucleotides. Binds hemimethylated DNA as well. Recruits histone deacetylases and DNA methyltransferases. Acts as transcriptional repressor and plays a role in gene silencing. Functions as a scaffold protein, targeting GATAD2A and GATAD2B to chromatin to promote repression. May enhance the activation of some unmethylated cAMP-responsive promoters.6 Publications

GO - Molecular functioni

  • C2H2 zinc finger domain binding Source: UniProtKB
  • chromatin binding Source: Ensembl
  • methyl-CpG binding Source: UniProtKB
  • mRNA binding Source: Ensembl
  • protein domain specific binding Source: UniProtKB
  • satellite DNA binding Source: ProtInc
  • siRNA binding Source: Ensembl

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiREACT_2232. RNA Polymerase I Promoter Opening.
REACT_263965. NoRC negatively regulates rRNA expression.

Names & Taxonomyi

Protein namesi
Recommended name:
Methyl-CpG-binding domain protein 2
Alternative name(s):
Demethylase
Short name:
DMTase
Methyl-CpG-binding protein MBD2
Gene namesi
Name:MBD2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 18

Organism-specific databases

HGNCiHGNC:6917. MBD2.

Subcellular locationi

  • Nucleus 2 Publications

  • Note: Nuclear, in discrete foci. Detected at replication foci in late S phase.

GO - Cellular componenti

  • cytoplasm Source: Ensembl
  • heterochromatin Source: Ensembl
  • histone deacetylase complex Source: Ensembl
  • nuclear chromatin Source: UniProtKB
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • protein complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30660.

Polymorphism and mutation databases

BioMutaiMBD2.
DMDMi50401198.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 411411Methyl-CpG-binding domain protein 2PRO_0000096260Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei181 – 1811Phosphoserine2 Publications
Modified residuei407 – 4071Phosphoserine5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UBB5.
PaxDbiQ9UBB5.
PRIDEiQ9UBB5.

PTM databases

PhosphoSiteiQ9UBB5.

Expressioni

Tissue specificityi

Highly expressed in brain, heart, kidney, stomach, testis and placenta.1 Publication

Gene expression databases

BgeeiQ9UBB5.
CleanExiHS_MBD2.
ExpressionAtlasiQ9UBB5. baseline and differential.
GenevisibleiQ9UBB5. HS.

Organism-specific databases

HPAiCAB037282.

Interactioni

Subunit structurei

Heterodimer with MBD3. Component of the MeCP1 complex that contains HDAC1 and HDAC2. Binds DNMT1, MIZF, GPN1, SIN3A, GATAD2A/p66-alpha and GATAD2B/p66-beta. Interacts with DHX9.10 Publications

Protein-protein interaction databases

BioGridi114445. 36 interactions.
IntActiQ9UBB5. 6 interactions.
MINTiMINT-210249.
STRINGi9606.ENSP00000256429.

Structurei

Secondary structure

1
411
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi366 – 38823Combined sources
Turni389 – 3924Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L2LNMR-B360-393[»]
ProteinModelPortaliQ9UBB5.
SMRiQ9UBB5. Positions 149-213, 360-393.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini145 – 21369MBDPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 149149Necessary for interaction with DHX9Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi6 – 140135Gly-richAdd
BLAST
Compositional biasi50 – 9647Arg-richAdd
BLAST

Sequence similaritiesi

Contains 1 MBD (methyl-CpG-binding) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG316386.
GeneTreeiENSGT00410000025376.
HOGENOMiHOG000013073.
HOVERGENiHBG052417.
InParanoidiQ9UBB5.
KOiK11590.
OMAiNCISICC.
OrthoDBiEOG7QNVMV.
PhylomeDBiQ9UBB5.
TreeFamiTF325032.

Family and domain databases

Gene3Di3.30.890.10. 2 hits.
InterProiIPR016177. DNA-bd_dom.
IPR025884. MeCpG-bd_2/3_C_dom.
IPR001739. Methyl_CpG_DNA-bd.
[Graphical view]
PfamiPF01429. MBD. 1 hit.
PF14048. MBD_C. 1 hit.
[Graphical view]
SMARTiSM00391. MBD. 1 hit.
[Graphical view]
SUPFAMiSSF54171. SSF54171. 1 hit.
PROSITEiPS50982. MBD. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UBB5-1) [UniParc]FASTAAdd to basket

Also known as: MBD2a, MBD2b

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MRAHPGGGRC CPEQEEGESA AGGSGAGGDS AIEQGGQGSA LAPSPVSGVR
60 70 80 90 100
REGARGGGRG RGRWKQAGRG GGVCGRGRGR GRGRGRGRGR GRGRGRPPSG
110 120 130 140 150
GSGLGGDGGG CGGGGSGGGG APRREPVPFP SGSAGPGPRG PRATESGKRM
160 170 180 190 200
DCPALPPGWK KEEVIRKSGL SAGKSDVYYF SPSGKKFRSK PQLARYLGNT
210 220 230 240 250
VDLSSFDFRT GKMMPSKLQK NKQRLRNDPL NQNKGKPDLN TTLPIRQTAS
260 270 280 290 300
IFKQPVTKVT NHPSNKVKSD PQRMNEQPRQ LFWEKRLQGL SASDVTEQII
310 320 330 340 350
KTMELPKGLQ GVGPGSNDET LLSAVASALH TSSAPITGQV SAAVEKNPAV
360 370 380 390 400
WLNTSQPLCK AFIVTDEDIR KQEERVQQVR KKLEEALMAD ILSRAADTEE
410
MDIEMDSGDE A
Length:411
Mass (Da):43,255
Last modified:May 1, 2000 - v1
Checksum:iFC4E5E0CF9BA0FFA
GO
Isoform 3 (identifier: Q9UBB5-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     235-302: GKPDLNTTLP...SDVTEQIIKT → LRWNTHRPAP...YSRQNQSFPP
     303-411: Missing.

Note: Incomplete sequence.
Show »
Length:302
Mass (Da):31,745
Checksum:iCCEC65D926222717
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei235 – 30268GKPDL…QIIKT → LRWNTHRPAPWHALSRLCLL IRCLLCLECAYPLPLHLVNS YSSKTQLHCLHLWEACPAYS RQNQSFPP in isoform 3. 1 PublicationVSP_011077Add
BLAST
Alternative sequencei303 – 411109Missing in isoform 3. 1 PublicationVSP_011078Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF072242 mRNA. Translation: AAC68871.1.
AF072246 mRNA. Translation: AAC68875.1.
AF120989, AF120988 Genomic DNA. Translation: AAD56596.1.
AF120993
, AF120988, AF120989, AF120990, AF120991, AF120992 Genomic DNA. Translation: AAD56597.1.
BC032638 mRNA. Translation: AAH32638.1.
CCDSiCCDS11953.1. [Q9UBB5-1]
CCDS45871.1. [Q9UBB5-3]
RefSeqiNP_003918.1. NM_003927.4. [Q9UBB5-1]
NP_056647.1. NM_015832.4. [Q9UBB5-3]
UniGeneiHs.25674.

Genome annotation databases

EnsembliENST00000256429; ENSP00000256429; ENSG00000134046. [Q9UBB5-1]
ENST00000583046; ENSP00000464554; ENSG00000134046. [Q9UBB5-3]
GeneIDi8932.
KEGGihsa:8932.
UCSCiuc002lfg.2. human. [Q9UBB5-1]
uc002lfh.2. human. [Q9UBB5-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF072242 mRNA. Translation: AAC68871.1.
AF072246 mRNA. Translation: AAC68875.1.
AF120989, AF120988 Genomic DNA. Translation: AAD56596.1.
AF120993
, AF120988, AF120989, AF120990, AF120991, AF120992 Genomic DNA. Translation: AAD56597.1.
BC032638 mRNA. Translation: AAH32638.1.
CCDSiCCDS11953.1. [Q9UBB5-1]
CCDS45871.1. [Q9UBB5-3]
RefSeqiNP_003918.1. NM_003927.4. [Q9UBB5-1]
NP_056647.1. NM_015832.4. [Q9UBB5-3]
UniGeneiHs.25674.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2L2LNMR-B360-393[»]
ProteinModelPortaliQ9UBB5.
SMRiQ9UBB5. Positions 149-213, 360-393.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114445. 36 interactions.
IntActiQ9UBB5. 6 interactions.
MINTiMINT-210249.
STRINGi9606.ENSP00000256429.

Chemistry

BindingDBiQ9UBB5.

PTM databases

PhosphoSiteiQ9UBB5.

Polymorphism and mutation databases

BioMutaiMBD2.
DMDMi50401198.

Proteomic databases

MaxQBiQ9UBB5.
PaxDbiQ9UBB5.
PRIDEiQ9UBB5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000256429; ENSP00000256429; ENSG00000134046. [Q9UBB5-1]
ENST00000583046; ENSP00000464554; ENSG00000134046. [Q9UBB5-3]
GeneIDi8932.
KEGGihsa:8932.
UCSCiuc002lfg.2. human. [Q9UBB5-1]
uc002lfh.2. human. [Q9UBB5-3]

Organism-specific databases

CTDi8932.
GeneCardsiGC18M051615.
HGNCiHGNC:6917. MBD2.
HPAiCAB037282.
MIMi603547. gene.
neXtProtiNX_Q9UBB5.
PharmGKBiPA30660.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG316386.
GeneTreeiENSGT00410000025376.
HOGENOMiHOG000013073.
HOVERGENiHBG052417.
InParanoidiQ9UBB5.
KOiK11590.
OMAiNCISICC.
OrthoDBiEOG7QNVMV.
PhylomeDBiQ9UBB5.
TreeFamiTF325032.

Enzyme and pathway databases

ReactomeiREACT_2232. RNA Polymerase I Promoter Opening.
REACT_263965. NoRC negatively regulates rRNA expression.

Miscellaneous databases

ChiTaRSiMBD2. human.
GeneWikiiMethyl-CpG-binding_domain_protein_2.
GenomeRNAii8932.
NextBioi33582.
PROiQ9UBB5.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UBB5.
CleanExiHS_MBD2.
ExpressionAtlasiQ9UBB5. baseline and differential.
GenevisibleiQ9UBB5. HS.

Family and domain databases

Gene3Di3.30.890.10. 2 hits.
InterProiIPR016177. DNA-bd_dom.
IPR025884. MeCpG-bd_2/3_C_dom.
IPR001739. Methyl_CpG_DNA-bd.
[Graphical view]
PfamiPF01429. MBD. 1 hit.
PF14048. MBD_C. 1 hit.
[Graphical view]
SMARTiSM00391. MBD. 1 hit.
[Graphical view]
SUPFAMiSSF54171. SSF54171. 1 hit.
PROSITEiPS50982. MBD. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Identification and characterization of a family of mammalian methyl-CpG binding proteins."
    Hendrich B., Bird A.
    Mol. Cell. Biol. 18:6538-6547(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), NUCLEOTIDE SEQUENCE [MRNA] OF 157-411 (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION.
    Tissue: Testis.
  2. "Genomic structure and chromosomal mapping of the murine and human mbd1, mbd2, mbd3, and mbd4 genes."
    Hendrich B., Abbott C., McQueen H., Chambers D., Cross S.H., Bird A.
    Mamm. Genome 10:906-912(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lymph.
  4. "A mammalian protein with specific demethylase activity for mCpG DNA."
    Bhattacharya S.K., Ramchandani S., Cervoni N., Szyf M.
    Nature 397:579-583(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 1), TISSUE SPECIFICITY.
  5. "MBD2 is a transcriptional repressor belonging to the MeCP1 histone deacetylase complex."
    Ng H.-H., Zhang Y., Hendrich B., Johnson C.A., Turner B.M., Erdjument-Bromage H., Tempst P., Reinberg D., Bird A.
    Nat. Genet. 23:58-61(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH MECP1 AND HDAC1.
  6. "MBD2-MBD3 complex binds to hemi-methylated DNA and forms a complex containing DNMT1 at the replication foci in late S phase."
    Tatematsu K., Yamazaki T., Ishikawa F.
    Genes Cells 5:677-688(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, HETERODIMERIZATION WITH MBD3, INTERACTION WITH DNMT1.
  7. "The minimal repression domain of MBD2b overlaps with the methyl-CpG-binding domain and binds directly to Sin3A."
    Boeke J., Ammerpohl O., Kegel S., Moehren U., Renkawitz R.
    J. Biol. Chem. 275:34963-34967(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION (ISOFORM 1), INTERACTION WITH SIN3A.
  8. "Stable histone deacetylase complexes distinguished by the presence of SANT domain proteins CoREST/kiaa0071 and Mta-L1."
    Humphrey G.W., Wang Y., Russanova V.R., Hirai T., Qin J., Nakatani Y., Howard B.H.
    J. Biol. Chem. 276:6817-6824(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HDAC1, IDENTIFICATION BY MASS SPECTROMETRY.
  9. "Involvement of a novel zinc finger protein, MIZF, in transcriptional repression by interacting with a methyl-CpG-binding protein, MBD2."
    Sekimata M., Takahashi A., Murakami-Sekimata A., Homma Y.
    J. Biol. Chem. 276:42632-42638(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MIZF.
  10. "Two highly related p66 proteins comprise a new family of potent transcriptional repressors interacting with MBD2 and MBD3."
    Brackertz M., Boeke J., Zhang R., Renkawitz R.
    J. Biol. Chem. 277:40958-40966(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH P66ALPHA AND P66BETA, SUBCELLULAR LOCATION.
  11. "MBDin, a novel MBD2-interacting protein, relieves MBD2 repression potential and reactivates transcription from methylated promoters."
    Lembo F., Pero R., Angrisano T., Vitiello C., Iuliano R., Bruni C.B., Chiariotti L.
    Mol. Cell. Biol. 23:1656-1665(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH GPN1.
  12. Cited for: FUNCTION, INTERACTION WITH DHX9.
  13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "p66alpha and p66beta of the Mi-2/NuRD complex mediate MBD2 and histone interaction."
    Brackertz M., Gong Z., Leers J., Renkawitz R.
    Nucleic Acids Res. 34:397-406(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH GATAD2A AND GATAD2B.
  15. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  16. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  17. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-181 AND SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "Probing the dynamic distribution of bound states for methylcytosine-binding domains on DNA."
    Cramer J.M., Scarsdale J.N., Walavalkar N.M., Buchwald W.A., Ginder G.D., Williams D.C. Jr.
    J. Biol. Chem. 289:1294-1302(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DNA-BINDING.
  20. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-407, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  21. "p66Alpha-MBD2 coiled-coil interaction and recruitment of Mi-2 are critical for globin gene silencing by the MBD2-NuRD complex."
    Gnanapragasam M.N., Scarsdale J.N., Amaya M.L., Webb H.D., Desai M.A., Walavalkar N.M., Wang S.Z., Zu Zhu S., Ginder G.D., Williams D.C. Jr.
    Proc. Natl. Acad. Sci. U.S.A. 108:7487-7492(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 360-393 IN COMPLEX WITH GATAD2A, SUBUNIT, INTERACTION WITH GATAD2A.

Entry informationi

Entry nameiMBD2_HUMAN
AccessioniPrimary (citable) accession number: Q9UBB5
Secondary accession number(s): O95242, Q9UIS8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: May 1, 2000
Last modified: June 24, 2015
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

Functional studies (PubMed:10050851, PubMed:10950960 and PubMed:12665568) have used a C-terminal fragment of isoform 1 which has been described originally as isoform MBD2b but cannot however be proven by supporting cDNA sequences.1 Publication

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 18
    Human chromosome 18: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.